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Bromine in PDB 5jf6: Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47)

Enzymatic activity of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47)

All present enzymatic activity of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47):
3.5.1.88;

Protein crystallography data

The structure of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47), PDB code: 5jf6 was solved by S.Fieulaine, C.Giglione, T.Meinnel, K.Hamiche, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.15 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.920, 66.280, 88.290, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 17.5

Other elements in 5jf6:

The structure of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47) also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47) (pdb code 5jf6). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47), PDB code: 5jf6:

Bromine binding site 1 out of 1 in 5jf6

Go back to Bromine Binding Sites List in 5jf6
Bromine binding site 1 out of 1 in the Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Type 2 Pdf From Streptococcus Agalactiae in Complex with Inhibitor 6B (AB47) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br301

b:21.9
occ:1.00
 BR A:BB4301 0.0 21.9 1.0
C8 A:BB4301 1.9 17.9 1.0
C7 A:BB4301 2.8 17.5 1.0
C9 A:BB4301 2.9 18.5 1.0
ND1 A:HIS174 3.7 8.1 1.0
CB A:HIS174 3.8 6.6 1.0
CG A:HIS174 3.8 7.0 1.0
O A:HOH801 4.0 25.2 1.0
CD A:GLU129 4.0 9.6 1.0
OE2 A:GLU129 4.1 8.8 1.0
CG2 A:ILE170 4.1 9.0 1.0
CA A:VAL171 4.1 8.3 1.0
C6 A:BB4301 4.1 17.9 1.0
CG2 A:VAL171 4.2 10.4 1.0
C10 A:BB4301 4.2 19.2 1.0
OE1 A:GLU129 4.3 8.3 1.0
CG A:GLU129 4.4 9.8 1.0
O A:ILE170 4.4 7.1 1.0
CE1 A:HIS174 4.5 8.4 1.0
N A:VAL171 4.5 7.7 1.0
CB A:VAL171 4.6 9.5 1.0
C A:ILE170 4.6 7.3 1.0
CD2 A:HIS174 4.6 8.0 1.0
CD1 A:LEU125 4.6 12.9 1.0
C11 A:BB4301 4.7 18.3 1.0
CB A:GLU129 4.9 9.9 1.0
NE2 A:HIS174 5.0 9.0 1.0

Reference:

S.Fieulaine, R.Alves De Sousa, L.Maigre, K.Hamiche, M.Alimi, J.M.Bolla, A.Taleb, A.Denis, J.M.Pages, I.Artaud, T.Meinnel, C.Giglione. A Unique Peptide Deformylase Platform to Rationally Design and Challenge Novel Active Compounds. Sci Rep V. 6 35429 2016.
ISSN: ESSN 2045-2322
PubMed: 27762275
DOI: 10.1038/SREP35429
Page generated: Thu Jul 11 00:06:46 2024

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